SMART: Pfam domain CAF1-p150

The domain within your query sequence starts at position 1 and ends at position 210; the E-value for the CAF1-p150_N domain shown below is 3.8e-59.

MLEEPEAATRTAAAVDCKDRPGFPVKRLIQARLPFKRLNLVPKEKVEEDTSPKAAVESKV
PDLQLSLGTFESQCHTGSHVGLSTKLVGGQGPIDSFLRATIKPVPSVVIIDLTENCSDIP
DSPEGHSELSPDTAGVVTTVEGAAKQQEHSAAELCLLETPSDITCHMEEEPGSPGDPKRT
GDCQAGSLQSCPELTPGSRTCPTKELSSWS

CAF1-p150_N

PFAM accession number:	PF15557
Interpro abstract (IPR029091):	Chromatin assembly factor 1 (CAF-1) consists of three evolutionary conserved subunits, p150, p60, and p48 (yeast homologues Cac1, cac2 and cac3 respectively), and mediates the assembly of nucleosomes onto newly replicated DNA. The p150 subunit (CAF-1_p150, also known as subunit A) is the core component of the CAF-1 histone chaperone complex, which functions in depositing newly synthesised and acetylated histones H3/H4 into chromatin during DNA replication and repair [ (PUBMED:14765118) (PUBMED:12697822) ], being essential for cell viability and efficient DNA replication. The p150 subunit contains the interaction regions with proliferating cell nuclear antigen (PCNA), heterochromatin protein 1 (HP1), the CAF-1 p60 subunit among others proteins [ (PUBMED:21209461) ]. It is thought that the DNA association with two histone-bound CAF-1 complexes may promote the formation of the (H3-H4)2 tetramer on DNA [ (PUBMED:28315523) ]. This entry represents the N-terminal region of the CAF-1 subunit p150 that contains one of the PCNA (proliferating cell nuclear antigen) binding sites, designated PIP1 and the heterochromatin protein 1 (HP1) interacting domain MIR [ (PUBMED:31586391) ]. These domains are dispensable for p150 role in nucleosome assembly and it is thought that this N-terminal region of CAF-1 might act as a regulatory domain contributing to CAF-1-PCNA interaction stability or mediate other functions during DNA repair or heterochromatin maintenance [ (PUBMED:21209461) ].

PFAM accession number:

PF15557

Interpro abstract (IPR029091):

Chromatin assembly factor 1 (CAF-1) consists of three evolutionary conserved subunits, p150, p60, and p48 (yeast homologues Cac1, cac2 and cac3 respectively), and mediates the assembly of nucleosomes onto newly replicated DNA. The p150 subunit (CAF-1_p150, also known as subunit A) is the core component of the CAF-1 histone chaperone complex, which functions in depositing newly synthesised and acetylated histones H3/H4 into chromatin during DNA replication and repair [ (PUBMED:14765118) (PUBMED:12697822) ], being essential for cell viability and efficient DNA replication. The p150 subunit contains the interaction regions with proliferating cell nuclear antigen (PCNA), heterochromatin protein 1 (HP1), the CAF-1 p60 subunit among others proteins [ (PUBMED:21209461) ]. It is thought that the DNA association with two histone-bound CAF-1 complexes may promote the formation of the (H3-H4)2 tetramer on DNA [ (PUBMED:28315523) ].

This entry represents the N-terminal region of the CAF-1 subunit p150 that contains one of the PCNA (proliferating cell nuclear antigen) binding sites, designated PIP1 and the heterochromatin protein 1 (HP1) interacting domain MIR [ (PUBMED:31586391) ]. These domains are dispensable for p150 role in nucleosome assembly and it is thought that this N-terminal region of CAF-1 might act as a regulatory domain contributing to CAF-1-PCNA interaction stability or mediate other functions during DNA repair or heterochromatin maintenance [ (PUBMED:21209461) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry CAF1-p150_N